ID A0A238XM85_9FLAO Unreviewed; 722 AA.
AC A0A238XM85;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Xylan alpha-1,2-glucuronidase {ECO:0000256|RuleBase:RU361198};
DE EC=3.2.1.131 {ECO:0000256|RuleBase:RU361198};
GN ORFNames=SAMN04488111_1882 {ECO:0000313|EMBL:SNR59089.1};
OS Lutibacter flavus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lutibacter.
OX NCBI_TaxID=691689 {ECO:0000313|EMBL:SNR59089.1, ECO:0000313|Proteomes:UP000198412};
RN [1] {ECO:0000313|Proteomes:UP000198412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27993 {ECO:0000313|Proteomes:UP000198412};
RA Varghese N., Submissions S.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->2)-alpha-D-(4-O-methyl)glucuronosyl links in
CC the main chain of hardwood xylans.; EC=3.2.1.131;
CC Evidence={ECO:0000256|RuleBase:RU361198};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU361198}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 67 family.
CC {ECO:0000256|ARBA:ARBA00008833, ECO:0000256|PIRNR:PIRNR029900,
CC ECO:0000256|RuleBase:RU361198}.
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DR EMBL; FZNX01000003; SNR59089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238XM85; -.
DR OrthoDB; 339499at2; -.
DR Proteomes; UP000198412; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0046559; F:alpha-glucuronidase activity; IEA:InterPro.
DR GO; GO:0033939; F:xylan alpha-1,2-glucuronosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1330.10; Alpha-glucuronidase, C-terminal domain; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR037054; A-glucoronidase_C_sf.
DR InterPro; IPR011395; Glyco_hydro_67_aGlcAse.
DR InterPro; IPR005154; Glyco_hydro_67_aGlcAse_N.
DR InterPro; IPR011099; Glyco_hydro_67_C.
DR InterPro; IPR011100; Glyco_hydro_67_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR PANTHER; PTHR39207; ALPHA-GLUCURONIDASE A; 1.
DR PANTHER; PTHR39207:SF1; ALPHA-GLUCURONIDASE A; 1.
DR Pfam; PF07477; Glyco_hydro_67C; 1.
DR Pfam; PF07488; Glyco_hydro_67M; 1.
DR Pfam; PF03648; Glyco_hydro_67N; 1.
DR PIRSF; PIRSF029900; Alpha-glucuronds; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361198};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR029900};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR029900};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361198};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000256|PIRNR:PIRNR029900}.
FT DOMAIN 31..152
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 156..475
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 476..700
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
FT ACT_SITE 313
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 387
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 415
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ SEQUENCE 722 AA; 82614 MW; 1A6F29A73367AF00 CRC64;
MTNFLSIKNF LVQLSILLLC LNVSAKDGYN LWLQYDYIQN NELRLAYKSN ISNILALGDS
ETMQVALNEL QLGLSKMLGT EILSQKDLKG ENLVIFGTQS NLDKKLIKKL KKELEQINNE
GFIIKQIIIK GKKHIIITGK TDVGVLYGVF NFLRIIQTHK SIKNIDVLDS PKVDIRMLNH
WDNLDRTVER GYAGFSLWDW HRLPDYIDSR YVDYARANAS VGINGTAITN VNANALILTP
QYLEKVEALA NVFRPYGLKV YLTARFSAPI EIGGLKTADP YDAEVINWWK EKTKEIYKRI
PDFGGFLVKA NSEGQPGPQN YGRNHVDGAN MLAEAVAPFG GIVMWRAFVY SEHDADDRAK
QAFSEFVPYD GQFKDNVIIQ VKNGAIDFQP REPFHPMFGA MPKTPLMMEF QITQEYLGFS
THLVYLPKLF EEVFEADTYR AGKGSTVAKV IDGSLHNKKI TGVAGVSNIG NDRNWTGHPF
LQANWYGYGR LAWNPHLNSG DIAEEWIRST FSNDTHFINP IKEMMLNSRE TVVNYMTPLG
LHHIMDTGHH YGPGPWVENL SRPEWNPVYY HKADKNGIGF DRTNSGSNAT NQYAPEVADI
FNNTATCPEK DLLWFHHLSW DYKLKDGNTL WDGIALKYQQ GVNEVETMVH TWKSLEKYVD
NQRFNEVEML LNIQHKESKW WRDACLLYFQ QFSEKELPEG VEKPIKTLEY FQSLKFPFAP
GN
//
